125653-69-2Relevant academic research and scientific papers
Highly enantioselective aminoacylase-catalyzed transesterification of secondary alcohols
Bakker,Spruijt,Van Rantwijk,Sheldon
, p. 1801 - 1808 (2007/10/03)
The aminoacylase (N-acyl-L-amino acid amidohydrolase; E.C. 3.5.1.14) from Aspergillus melleus, a readily available inexpensive enzyme, catalyzes the transesterification of a wide range of chiral secondary arylalkanols with essentially absolute stereoselectivity (E> 500). Moreover, the productivities obtained with 1-phenylethanol, 1-phenylpropanol, 1-(1-naphthyl)ethanol and 1- (2-naphthyl)ethanol were substantially higher than those in the corresponding lipase-catalyzed transesterifications. (C) 2000 Elsevier Science Ltd.
The development of non-steroidal dual inhibitors of both human 5α- reductase isozymes
Blagg,Ballard,Cooper,Finn,Johnson,MacIntyre,Maw,Spargo
, p. 1517 - 1522 (2007/10/03)
The design, synthesis and biological properties of homochiral non- steroidal inhibitors of both isozymes of human 5α-reductase are described. The o-hydroxy aniline moiety of the initial lead (1) can be replaced by a 3- acyl indole isostere, whilst the minimum energy conformation of the benzyl ether in the potent inhibitor (3) is mimicked by the conformationally locked benzodioxolane system in the potent non-steroidal inhibitor (7). Pharmacokinetics and oral efficacy in a rat model of BPH are presented for (3) and (7).
LIPASE-CATALYZED IRREVERSIBLE TRANSESTERIFICATION USING ENOL ESTERS: XAD-8 IMMOBILIZED LIPOPROTEIN LIPASE-CATALYZED RESOLUTION OF SECONDARY ALCOHOLS
Hsu, Shu-Hui,Wu, Shihn-Sheng,Wang, Yi-Fong,Wong, Chi-Huey
, p. 6403 - 6406 (2007/10/02)
Procedures for preparation of XAD-8 immobilized lipoprotein lipase and the resolution of secondary alcohols of synthetic value in organic solvents using this immobilized enzyme have been developed.
